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Q9UL25 (RAB21_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ras-related protein Rab-21
Gene names
Name:RAB21
Synonyms:KIAA0118
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length225 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Regulates integrin internalization and recycling, but does not influence the traffic of endosomally translocated receptors in general. As a result, may regulate cell adhesion and migration By similarity. During the mitosis of adherent cells, controls the endosomal trafficking of integrins which is required for the successful completion of cytokinesis. Ref.6

Subunit structure

Interacts with the cytoplasmic tail of integrins ITGA1, ITGA2, ITGA5, ITGA6, ITGA11 and ITGB1 By similarity. Interacts with RABGEF1 (via VPS9 domain).

Subcellular location

Endoplasmic reticulum membrane; Lipid-anchor By similarity. Golgi apparatus membrane. Early endosome membrane. Cytoplasmic vesicle membrane. Cleavage furrow. Note: In nonpolarized epithelial Caco-2 cells, found in the endoplasmic reticulum; in polarized cells, observed in vesicles in the apical cytoplasm. During mitosis, in mid-telophase, localized in the ingressing cleavage furrow. In late telophase, detected at the opposite poles of the daughter cells, in vesicles at the base of lamellipodia formed by the separating daughter cells. Ref.1 Ref.5 Ref.6

Tissue specificity

Widely expressed. In jejunal tissue, predominantly expressed in the apical region of the epithelial cell layer of the villi, weak expression, if any, in the crypt epithelium. Capillary endothelium and some cell types in the lamina propria also show expression. Ref.1

Sequence similarities

Belongs to the small GTPase superfamily. Rab family.

Ontologies

Keywords
   Biological processProtein transport
Transport
   Cellular componentCytoplasmic vesicle
Endoplasmic reticulum
Endosome
Golgi apparatus
Membrane
   LigandGTP-binding
Nucleotide-binding
   PTMAcetylation
Lipoprotein
Methylation
Prenylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processGTP catabolic process

Inferred from direct assay Ref.10. Source: GOC

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

small GTPase mediated signal transduction

Inferred from electronic annotation. Source: InterPro

   Cellular_componentGolgi membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

cleavage furrow

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasmic vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

early endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

endosome

Inferred from direct assay. Source: LIFEdb

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 20458337PubMed 23376485. Source: UniProt

   Molecular_functionGDP binding

Inferred from direct assay Ref.10PubMed 20937701. Source: UniProtKB

GTP binding

Inferred from direct assay Ref.10. Source: UniProtKB

GTPase activity

Inferred from direct assay Ref.10. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.11. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

APPL1Q9UKG110EBI-1056039,EBI-741243

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 222221Ras-related protein Rab-21
PRO_0000121205
Propeptide223 – 2253Removed in mature form Potential
PRO_0000370768

Regions

Nucleotide binding26 – 349GTP
Nucleotide binding74 – 785GTP By similarity
Nucleotide binding132 – 1354GTP
Nucleotide binding162 – 1643GTP
Motif48 – 569Effector region By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.3 Ref.7 Ref.9
Modified residue2221Cysteine methyl ester Potential
Lipidation2211S-geranylgeranyl cysteine By similarity
Lipidation2221S-geranylgeranyl cysteine By similarity

Experimental info

Mutagenesis331T → N: Defects in GTP-binding. Ref.5
Mutagenesis781Q → L: Defects in GTP hydrolysis. Ref.5

Secondary structure

............................... 225
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9UL25 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 73CA2C127F0CBFD6

FASTA22524,348
        10         20         30         40         50         60 
MAAAGGGGGG AAAAGRAYSF KVVLLGEGCV GKTSLVLRYC ENKFNDKHIT TLQASFLTKK 

        70         80         90        100        110        120 
LNIGGKRVNL AIWDTAGQER FHALGPIYYR DSNGAILVYD ITDEDSFQKV KNWVKELRKM 

       130        140        150        160        170        180 
LGNEICLCIV GNKIDLEKER HVSIQEAESY AESVGAKHYH TSAKQNKGIE ELFLDLCKRM 

       190        200        210        220 
IETAQVDERA KGNGSSQPGT ARRGVQIIDD EPQAQTSGGG CCSSG 

« Hide

References

« Hide 'large scale' references
[1]"Expression of Rab small GTPases in epithelial Caco-2 cells: Rab21 is an apically located GTP-binding protein in polarised intestinal epithelial cells."
Opdam F.J.M., Kamps G., Croes H., van Bokhoven H., Ginsel L.A., Fransen J.A.M.
Eur. J. Cell Biol. 79:308-316(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Colon carcinoma.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lymph and Placenta.
[3]Bienvenut W.V.
Submitted (JUN-2005) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-16; 48-59; 91-109 AND 141-157, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: B-cell lymphoma.
[4]"Prediction of the coding sequences of unidentified human genes. III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of cDNA clones from human cell line KG-1."
Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S., Tabata S., Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.
DNA Res. 2:37-43(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 65-225.
Tissue: Bone marrow.
[5]"A role for the small GTPase Rab21 in the early endocytic pathway."
Simpson J.C., Griffiths G., Wessling-Resnick M., Fransen J.A.M., Bennett H., Jones A.T.
J. Cell Sci. 117:6297-6311(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF THR-33 AND GLN-78.
[6]"Integrin trafficking regulated by Rab21 is necessary for cytokinesis."
Pellinen T., Tuomi S., Arjonen A., Wolf M., Edgren H., Meyer H., Grosse R., Kitzing T., Rantala J.K., Kallioniemi O., Faessler R., Kallio M., Ivaska J.
Dev. Cell 15:371-385(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[7]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Structural basis of family-wide Rab GTPase recognition by rabenosyn-5."
Eathiraj S., Pan X., Ritacco C., Lambright D.G.
Nature 436:415-419(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 16-183 IN COMPLEX WITH GTP ANALOG AND GDP.
[11]"Structural basis for Rab GTPase activation by VPS9 domain exchange factors."
Delprato A., Lambright D.G.
Nat. Struct. Mol. Biol. 14:406-412(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 16-183 IN COMPLEX WITH RABGEF1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF091035 mRNA. Translation: AAF00048.1.
BC021901 mRNA. Translation: AAH21901.1.
BC092475 mRNA. Translation: AAH92475.1.
D42087 mRNA. Translation: BAA07682.1.
CCDSCCDS9003.1.
RefSeqNP_055814.1. NM_014999.2.
UniGeneHs.524590.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1YZTX-ray2.05A/B16-183[»]
1YZUX-ray2.50A/B16-183[»]
1Z08X-ray1.80A/B/C/D16-183[»]
1Z0IX-ray2.33A16-183[»]
2OT3X-ray2.10B16-183[»]
ProteinModelPortalQ9UL25.
SMRQ9UL25. Positions 17-181.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116653. 6 interactions.
DIPDIP-29349N.
IntActQ9UL25. 5 interactions.
MINTMINT-3081967.
STRING9606.ENSP00000261263.

PTM databases

PhosphoSiteQ9UL25.

Polymorphism databases

DMDM13633613.

Proteomic databases

MaxQBQ9UL25.
PaxDbQ9UL25.
PeptideAtlasQ9UL25.
PRIDEQ9UL25.

Protocols and materials databases

DNASU23011.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000261263; ENSP00000261263; ENSG00000080371.
GeneID23011.
KEGGhsa:23011.
UCSCuc001swt.3. human.

Organism-specific databases

CTD23011.
GeneCardsGC12P072100.
HGNCHGNC:18263. RAB21.
HPACAB037048.
HPA016988.
MIM612398. gene.
neXtProtNX_Q9UL25.
PharmGKBPA34111.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1100.
HOGENOMHOG000233968.
HOVERGENHBG009351.
InParanoidQ9UL25.
KOK07890.
OMASHFFASA.
OrthoDBEOG7RZ5QX.
PhylomeDBQ9UL25.
TreeFamTF300199.

Enzyme and pathway databases

BRENDA3.6.5.2. 2681.

Gene expression databases

ArrayExpressQ9UL25.
BgeeQ9UL25.
CleanExHS_RAB21.
GenevestigatorQ9UL25.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view]
PfamPF00071. Ras. 1 hit.
[Graphical view]
PRINTSPR00449. RASTRNSFRMNG.
SMARTSM00175. RAB. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00231. small_GTP. 1 hit.
PROSITEPS51419. RAB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRAB21. human.
EvolutionaryTraceQ9UL25.
GeneWikiRAB21.
GenomeRNAi23011.
NextBio43928.
PROQ9UL25.
SOURCESearch...

Entry information

Entry nameRAB21_HUMAN
AccessionPrimary (citable) accession number: Q9UL25
Secondary accession number(s): Q14466, Q569H3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 139 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM